This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4k1o
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4k1o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K1O FirstGlance]. <br> | <table><tr><td colspan='2'>[[4k1o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K1O FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.603Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4k1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k1o OCA], [https://pdbe.org/4k1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k1o RCSB], [https://www.ebi.ac.uk/pdbsum/4k1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k1o ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4k1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k1o OCA], [https://pdbe.org/4k1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k1o RCSB], [https://www.ebi.ac.uk/pdbsum/4k1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k1o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CTNA2_MOUSE CTNA2_MOUSE] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.<ref>PMID:12089526</ref> <ref>PMID:12123610</ref> <ref>PMID:15034585</ref> | [https://www.uniprot.org/uniprot/CTNA2_MOUSE CTNA2_MOUSE] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.<ref>PMID:12089526</ref> <ref>PMID:12123610</ref> <ref>PMID:15034585</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | alpha-catenin is an actin- and vinculin-binding protein that regulates cell-cell adhesion by interacting with cadherin adhesion receptors through beta-catenin, but the mechanisms by which it anchors the cadherin-catenin complex to the actin cytoskeleton at adherens junctions remain unclear. Here we determined crystal structures of alphaE-catenin in the autoinhibited state and the actin-binding domain of alphaN-catenin. Together with the small-angle X-ray scattering analysis of full-length alphaN-catenin, we deduced an elongated multidomain assembly of monomeric alpha-catenin that structurally and functionally couples the vinculin- and actin-binding mechanisms. Cellular and biochemical studies of alphaE- and alphaN-catenins show that alphaE-catenin recruits vinculin to adherens junctions more effectively than alphaN-catenin, partly owing to its higher affinity for actin filaments. We propose a molecular switch mechanism involving multi-state conformational changes of alpha-catenin. This would be driven by actomyosin-generated tension to dynamically regulate the vinculin-assisted linkage between adherens junctions and the actin cytoskeleton. | ||
| - | |||
| - | An Autoinhibited Structure of alpha-catenin and Its Implications for Vinculin Recruitment to Adherens Junctions.,Ishiyama N, Tanaka N, Abe K, Yang YJ, Abbas YM, Umitsu M, Nagar B, Bueler SA, Rubinstein JL, Takeichi M, Ikura M J Biol Chem. 2013 Apr 15. PMID:23589308<ref>PMID:23589308</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4k1o" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Crystal structure of the alphaN-catenin actin-binding domain
| |||||||||||
